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http://purl.uniprot.org/citations/10704359http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10704359http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10704359http://www.w3.org/2000/01/rdf-schema#comment"Phosphorylation of the negative-sense RNA virus phosphoproteins is highly conserved, implying functional significance. Sendai virus (SV) phosphoprotein (P) is constitutively phosphorylated at S249. Abrogation of the SV P primary phosphorylation causes phosphorylation of P at alternate sites, creating a problem in determining the function of phosphorylation. We have now identified the alternate phosphorylation sites using two-dimensional phosphopeptide analysis of several deletion and point mutants of the P protein. The alternate phosphorylation sites were mutagenized to create P with (S249combo) or without (combo) primary phosphorylation. The combo protein has less than 10% phosphorylation compared with the wild-type P or S249combo. Functional analysis of the mutant proteins using a Sendai virus minigenome replication system showed that the combo P protein was as proficient in supporting minigenome replication as the wild-type P in cell cultures. These studies suggest that like the primary, the alternate phosphorylation of the P protein is also dispensable for virus replication in cell cultures. Interestingly, the ability of the multiple site mutant of P (combo mutant has eight serine residues changed to alanine residues) to support efficient virus RNA synthesis suggests that the P protein has a high flexibility at least in its sequence and perhaps also in structure."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.org/dc/terms/identifier"doi:10.1006/viro.1999.0176"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.org/dc/terms/identifier"doi:10.1006/viro.1999.0176"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/author"Gupta K.C."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/author"Gupta K.C."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/author"Hu C.-J."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/author"Hu C.-J."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/name"Virology"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/name"Virology"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/pages"517-532"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/pages"517-532"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/title"Functional significance of alternate phosphorylation in Sendai virus P protein."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/title"Functional significance of alternate phosphorylation in Sendai virus P protein."xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/volume"268"xsd:string
http://purl.uniprot.org/citations/10704359http://purl.uniprot.org/core/volume"268"xsd:string
http://purl.uniprot.org/citations/10704359http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10704359
http://purl.uniprot.org/citations/10704359http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10704359
http://purl.uniprot.org/citations/10704359http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10704359
http://purl.uniprot.org/citations/10704359http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10704359
http://purl.uniprot.org/uniprot/P04859http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10704359
http://purl.uniprot.org/uniprot/P04859#attribution-52D7FAC4848EE7448D26A6BAE5150709http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10704359